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Protein

Ras-related protein Rab-21

Gene

RAB21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general. As a result, may regulate cell adhesion and migration (By similarity). During the mitosis of adherent cells, controls the endosomal trafficking of integrins which is required for the successful completion of cytokinesis. Involved in neurite growth (By similarity).By similarity1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi26 – 349GTP
Nucleotide bindingi74 – 785GTPBy similarity
Nucleotide bindingi132 – 1354GTP
Nucleotide bindingi162 – 1643GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: GO_Central
  2. metabolic process Source: GOC
  3. positive regulation of early endosome to late endosome transport Source: UniProtKB
  4. positive regulation of receptor-mediated endocytosis Source: UniProtKB
  5. Rab protein signal transduction Source: GO_Central
  6. regulation of endocytosis Source: GO_Central
  7. regulation of exocytosis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.5.2. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-21
Gene namesi
Name:RAB21
Synonyms:KIAA0118
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:18263. RAB21.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity. Golgi apparatustrans-Golgi network 1 Publication. Golgi apparatus membrane. Early endosome membrane. Cytoplasmic vesicle membrane. Cleavage furrow
Note: Colocalizes with ANKRD27 and VAMP7 in neurites (By similarity). In nonpolarized epithelial Caco-2 cells, found in the endoplasmic reticulum; in polarized cells, observed in vesicles in the apical cytoplasm. During mitosis, in mid-telophase, localized in the ingressing cleavage furrow. In late telophase, detected at the opposite poles of the daughter cells, in vesicles at the base of lamellipodia formed by the separating daughter cells.By similarity

GO - Cellular componenti

  1. cleavage furrow Source: UniProtKB-SubCell
  2. cytoplasmic side of early endosome membrane Source: UniProtKB
  3. cytoplasmic side of plasma membrane Source: UniProtKB
  4. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
  5. early endosome Source: GO_Central
  6. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  7. endosome Source: LIFEdb
  8. extracellular vesicular exosome Source: UniProtKB
  9. focal adhesion Source: UniProtKB
  10. Golgi cisterna membrane Source: UniProtKB
  11. trans-Golgi network Source: UniProtKB
  12. vesicle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331T → N: Defects in GTP-binding. 1 Publication
Mutagenesisi78 – 781Q → L: Defects in GTP hydrolysis. 1 Publication

Organism-specific databases

PharmGKBiPA34111.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 222221Ras-related protein Rab-21PRO_0000121205Add
BLAST
Propeptidei223 – 2253Removed in mature formSequence AnalysisPRO_0000370768

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Lipidationi221 – 2211S-geranylgeranyl cysteineBy similarity
Modified residuei222 – 2221Cysteine methyl esterSequence Analysis
Lipidationi222 – 2221S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ9UL25.
PaxDbiQ9UL25.
PeptideAtlasiQ9UL25.
PRIDEiQ9UL25.

PTM databases

PhosphoSiteiQ9UL25.

Expressioni

Tissue specificityi

Widely expressed. In jejunal tissue, predominantly expressed in the apical region of the epithelial cell layer of the villi, weak expression, if any, in the crypt epithelium. Capillary endothelium and some cell types in the lamina propria also show expression.1 Publication

Gene expression databases

BgeeiQ9UL25.
CleanExiHS_RAB21.
ExpressionAtlasiQ9UL25. baseline and differential.
GenevestigatoriQ9UL25.

Organism-specific databases

HPAiCAB037048.
HPA016988.

Interactioni

Subunit structurei

Interacts with the cytoplasmic tail of integrins ITGA1, ITGA2, ITGA5, ITGA6, ITGA11 and ITGB1 (By similarity). Interacts with RABGEF1 (via VPS9 domain). Interacts with ANKRD27 (PubMed:16525121, PubMed:18477474).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPL1Q9UKG110EBI-1056039,EBI-741243

Protein-protein interaction databases

BioGridi116653. 8 interactions.
DIPiDIP-29349N.
IntActiQ9UL25. 5 interactions.
MINTiMINT-3081967.
STRINGi9606.ENSP00000261263.

Structurei

Secondary structure

1
225
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258Combined sources
Helixi28 – 303Combined sources
Helixi32 – 4110Combined sources
Beta strandi46 – 483Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi67 – 748Combined sources
Helixi79 – 846Combined sources
Helixi85 – 895Combined sources
Beta strandi93 – 1008Combined sources
Helixi104 – 12118Combined sources
Helixi122 – 1243Combined sources
Beta strandi125 – 1328Combined sources
Helixi134 – 1396Combined sources
Helixi144 – 15310Combined sources
Beta strandi157 – 1626Combined sources
Turni163 – 1664Combined sources
Helixi169 – 18113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZTX-ray2.05A/B16-183[»]
1YZUX-ray2.50A/B16-183[»]
1Z08X-ray1.80A/B/C/D16-183[»]
1Z0IX-ray2.33A16-183[»]
2OT3X-ray2.10B16-183[»]
ProteinModelPortaliQ9UL25.
SMRiQ9UL25. Positions 17-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UL25.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi48 – 569Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9UL25.
KOiK07890.
OMAiSHFFASA.
OrthoDBiEOG7RZ5QX.
PhylomeDBiQ9UL25.
TreeFamiTF300199.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9UL25-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAGGGGGG AAAAGRAYSF KVVLLGEGCV GKTSLVLRYC ENKFNDKHIT
60 70 80 90 100
TLQASFLTKK LNIGGKRVNL AIWDTAGQER FHALGPIYYR DSNGAILVYD
110 120 130 140 150
ITDEDSFQKV KNWVKELRKM LGNEICLCIV GNKIDLEKER HVSIQEAESY
160 170 180 190 200
AESVGAKHYH TSAKQNKGIE ELFLDLCKRM IETAQVDERA KGNGSSQPGT
210 220
ARRGVQIIDD EPQAQTSGGG CCSSG
Length:225
Mass (Da):24,348
Last modified:January 22, 2007 - v3
Checksum:i73CA2C127F0CBFD6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091035 mRNA. Translation: AAF00048.1.
BC021901 mRNA. Translation: AAH21901.1.
BC092475 mRNA. Translation: AAH92475.1.
D42087 mRNA. Translation: BAA07682.1.
CCDSiCCDS9003.1.
RefSeqiNP_055814.1. NM_014999.2.
UniGeneiHs.524590.

Genome annotation databases

EnsembliENST00000261263; ENSP00000261263; ENSG00000080371.
GeneIDi23011.
KEGGihsa:23011.
UCSCiuc001swt.3. human.

Polymorphism databases

DMDMi13633613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091035 mRNA. Translation: AAF00048.1.
BC021901 mRNA. Translation: AAH21901.1.
BC092475 mRNA. Translation: AAH92475.1.
D42087 mRNA. Translation: BAA07682.1.
CCDSiCCDS9003.1.
RefSeqiNP_055814.1. NM_014999.2.
UniGeneiHs.524590.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YZTX-ray2.05A/B16-183[»]
1YZUX-ray2.50A/B16-183[»]
1Z08X-ray1.80A/B/C/D16-183[»]
1Z0IX-ray2.33A16-183[»]
2OT3X-ray2.10B16-183[»]
ProteinModelPortaliQ9UL25.
SMRiQ9UL25. Positions 17-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116653. 8 interactions.
DIPiDIP-29349N.
IntActiQ9UL25. 5 interactions.
MINTiMINT-3081967.
STRINGi9606.ENSP00000261263.

PTM databases

PhosphoSiteiQ9UL25.

Polymorphism databases

DMDMi13633613.

Proteomic databases

MaxQBiQ9UL25.
PaxDbiQ9UL25.
PeptideAtlasiQ9UL25.
PRIDEiQ9UL25.

Protocols and materials databases

DNASUi23011.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261263; ENSP00000261263; ENSG00000080371.
GeneIDi23011.
KEGGihsa:23011.
UCSCiuc001swt.3. human.

Organism-specific databases

CTDi23011.
GeneCardsiGC12P072100.
HGNCiHGNC:18263. RAB21.
HPAiCAB037048.
HPA016988.
MIMi612398. gene.
neXtProtiNX_Q9UL25.
PharmGKBiPA34111.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00760000119101.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9UL25.
KOiK07890.
OMAiSHFFASA.
OrthoDBiEOG7RZ5QX.
PhylomeDBiQ9UL25.
TreeFamiTF300199.

Enzyme and pathway databases

BRENDAi3.6.5.2. 2681.

Miscellaneous databases

ChiTaRSiRAB21. human.
EvolutionaryTraceiQ9UL25.
GeneWikiiRAB21.
GenomeRNAii23011.
NextBioi43928.
PROiQ9UL25.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UL25.
CleanExiHS_RAB21.
ExpressionAtlasiQ9UL25. baseline and differential.
GenevestigatoriQ9UL25.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression of Rab small GTPases in epithelial Caco-2 cells: Rab21 is an apically located GTP-binding protein in polarised intestinal epithelial cells."
    Opdam F.J.M., Kamps G., Croes H., van Bokhoven H., Ginsel L.A., Fransen J.A.M.
    Eur. J. Cell Biol. 79:308-316(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Colon carcinoma.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph and Placenta.
  3. Bienvenut W.V.
    Submitted (MAY-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-16; 48-59; 91-109 AND 141-157, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  4. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-225.
    Tissue: Bone marrow.
  5. Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF THR-33 AND GLN-78.
  6. "Varp is a Rab21 guanine nucleotide exchange factor and regulates endosome dynamics."
    Zhang X., He X., Fu X.-Y., Chang Z.
    J. Cell Sci. 119:1053-1062(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD27.
  7. "Varp interacts with Rab38 and functions as its potential effector."
    Wang F., Zhang H., Zhang X., Wang Y., Ren F., Zhang X., Zhai Y., Chang Z.
    Biochem. Biophys. Res. Commun. 372:162-167(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD27.
  8. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "Role of Varp, a Rab21 exchange factor and TI-VAMP/VAMP7 partner, in neurite growth."
    Burgo A., Sotirakis E., Simmler M.C., Verraes A., Chamot C., Simpson J.C., Lanzetti L., Proux-Gillardeaux V., Galli T.
    EMBO Rep. 10:1117-1124(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "Structural basis of family-wide Rab GTPase recognition by rabenosyn-5."
    Eathiraj S., Pan X., Ritacco C., Lambright D.G.
    Nature 436:415-419(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 16-183 IN COMPLEX WITH GTP ANALOG AND GDP.
  14. "Structural basis for Rab GTPase activation by VPS9 domain exchange factors."
    Delprato A., Lambright D.G.
    Nat. Struct. Mol. Biol. 14:406-412(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 16-183 IN COMPLEX WITH RABGEF1.

Entry informationi

Entry nameiRAB21_HUMAN
AccessioniPrimary (citable) accession number: Q9UL25
Secondary accession number(s): Q14466, Q569H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2001
Last sequence update: January 22, 2007
Last modified: March 3, 2015
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.